1leh: Difference between revisions

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[[Image:1leh.gif|left|200px]]


{{Structure
==LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS==
|PDB= 1leh |SIZE=350|CAPTION= <scene name='initialview01'>1leh</scene>, resolution 2.2&Aring;
<StructureSection load='1leh' size='340' side='right'caption='[[1leh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1leh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LEH FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Leucine_dehydrogenase Leucine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.9 1.4.1.9]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1leh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1leh OCA], [https://pdbe.org/1leh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1leh RCSB], [https://www.ebi.ac.uk/pdbsum/1leh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1leh ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS'''
[https://www.uniprot.org/uniprot/Q7SIB4_LYSSH Q7SIB4_LYSSH]
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
BACKGROUND: Glutamate, phenylalanine and leucine dehydrogenases catalyze the NAD(P)(+)-linked oxidative deamination of L-amino acids to the corresponding 2-oxoacids, and sequence homology between these enzymes clearly indicates the existence of an enzyme superfamily related by divergent evolution. We have undertaken structural studies on a number of members of this family in order to investigate the molecular basis of their differential amino acid specificity. RESULTS: We have solved the X-ray structure of the leucine dehydrogenase from Bacillus sphaericus to a resolution of 2.2 A. Each subunit of this octameric enzyme contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. CONCLUSIONS: Comparison of the structure of leucine dehydrogenase with a hexameric glutamate dehydrogenase has shown that these two enzymes share a related fold and possess a similar catalytic chemistry. A mechanism for the basis of the differential amino acid specificity between these enzymes involves point mutations in the amino acid side-chain specificity pocket and subtle changes in the shape of this pocket caused by the differences in quaternary structure.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/le/1leh_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1LEH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEH OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1leh ConSurf].
A role for quaternary structure in the substrate specificity of leucine dehydrogenase., Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW, Structure. 1995 Jul 15;3(7):693-705. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8591046 8591046]
<div style="clear:both"></div>
[[Category: Leucine dehydrogenase]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Single protein]]
[[Category: Baker PJ]]
[[Category: Baker, P J.]]
[[Category: Rice DW]]
[[Category: Rice, D W.]]
[[Category: Sedelnikova SE]]
[[Category: Sedelnikova, S E.]]
[[Category: Stillman TJ]]
[[Category: Stillman, T J.]]
[[Category: Turnbull AP]]
[[Category: Turnbull, A P.]]
[[Category: oxidoreductase]]
 
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Retrieved from "https://proteopedia.org/1leh"